Cloning, purification and biochemical properties of a thermostable pectinase from Bacillus halodurans M29

Mei, Yan‐Zhen; Chen, Yuru; Zhai, Ruying; Liu, Yang

doi:10.1016/j.molcatb.2013.05.004

Cited by 37 publications

(28 citation statements)

References 23 publications

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“…At 60°C, it maintained 47 % of residual activity for 45 min. The characteristics of alkaline pectinase of B. mojavensis I4 are comparable to those of B. halodurans M29 that was optimally active at pH 10.0 and 80°C (Mei et al 2013), the pectinase from B. pumilus dcsr1 reported to exhibits maximal activity at pH 10.5 and 50°C (Sharma and Satyanarayana 2006) and also pectate lyase from B. tequilensis SV11 which kept maximum activity at pH 9.0 and 60°C (Chiliveri and Linga 2014).…”

Section: Biochemical Propertiesmentioning

confidence: 69%

Assessment of pectinase production by Bacillus mojavensis I4 using an economical substrate and its potential application in oil sesame extraction

et al. 2015

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Carrot (Daucus carota) peels, local agricultural waste product, is rich in lignocellulolytic material, including pectin which can act as an inducer of pectinase production. Pectinolytic enzymes production by Bacillus mojavensis I4 was studied in liquid state fermentation using carrot peel as a substrate. Medium composition and culture conditions for the pectinase production by I4 were optimized using two statistical methods: Taguchi design was applied to find the key ingredients and conditions for the best yield of enzyme production and The Box-Behnken design was used to optimize the value of the four significant variables: carrot peels powder, NH4Cl, inoculum size and incubation time. The optimal conditions for higher production of pectinase were carrot peels powder 6.5 %, NH4Cl 0.3 %, inoculum level 3 % and cultivation time 32 h. Under these conditions, the pectinase experimental yield (64.8 U/ml) closely matched the yield predicted by the statistical model (63.55 U/ml) with R (2) = 0.963. The best pectinase activity was observed at the temperature of 60 °C and at pH 8.0. The enzyme retained more than 90 % of its activity after 24 h at pH ranging from 6.0 to 10.0. The enzyme preserved more than 85 % of its initial activity after 60 min of pre-incubation at 30-40 °C and more than 67 % at 50 °C. The extracellular juice of I4 was applied in the process of sesame seeds oil extraction. An improvement of 3 % on the oil yield was obtained. The findings demonstrated that the B. mojavensis I4 has a promising potential for future use in a wide range of industrial and biotechnological applications.

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Section: Biochemical Propertiesmentioning

confidence: 69%

Assessment of pectinase production by Bacillus mojavensis I4 using an economical substrate and its potential application in oil sesame extraction

et al. 2015

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“…Caratovora BR1 had molecular mass of 43 kD. [20] Molecular masses of pectinase from other microbial sources were also found to be in a similar range: Bacillus halodurans (44 kD), [21] Tetracoccosporium sp. (36 kD), [22] Rhizopus sp.…”

Section: Purification and Characterization Of Marine Pectinasementioning

confidence: 99%

Characterization, Kinetic, and Thermodynamic Studies of Marine Pectinase FromBacillus subtilis

Joshi

Nerurkar

Adivarekar

2014

Preparative Biochemistry and Biotechnology

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Characterization, kinetic and thermodynamic parameters of purified pectinase from Bacillus subtilis, isolated from a marine sediment sample collected from Chinchani beach at Tarapore, India, were studied. Marine pectinase produced under submerged growth conditions was purified by ammonium sulfate precipitation followed by gel filtration chromatography using DEAE cellulose. Partial characterization of the marine pectinase was carried out in terms of effect of pH, temperature, substrate concentration, and metal ions. It was found that pectinase from marine B. subtilis showed maximal activity in alkaline buffer at pH 9.0 and at 40°C. It was also found that metal ions, namely, Mn(2+) and Fe(2+), stimulate pectinase activity. Marine pectinase followed Michaelis-Menten kinetics. The kinetics and thermodynamic parameters of the purified marine pectinase from B. subtilis were studied as the characterization of the enzyme is vital for its use in industrial processes.

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“…Surfactant agent stability of the enzyme is one of the important parameters enabling enzymes to be used in different types of industries, especially the detergent industry [15]. Thus, achieving the highest surfactant agent stability of the enzyme is one of the main goals for optimization of any pectinase extraction procedure.…”

Section: Surfactant Agent Stabilitymentioning

confidence: 99%

“…After incubation, the residual activity of pectinase was measured by polygalactouronic acid at pH 4.5 at 37 °C [15,22].…”

Section: Determination Of Temperature Stabilitymentioning

confidence: 99%

Optimization of Extraction of Novel Pectinase Enzyme Discovered in Red Pitaya (Hylocereus polyrhizus) Peel

Zohdi

Amid

2013

Molecules

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Plant peels could be a potential source of novel pectinases for use in various industrial applications due to their broad substrate specificity with high stability under extreme conditions. Therefore, the extraction conditions of a novel pectinase enzyme from pitaya peel was optimized in this study. The effect of extraction variables, namely buffer to sample ratio (2:1 to 8:1, X 1 ), extraction temperature (−15 to +25 °C, X 2 ) and buffer pH (4.0 to 12.0, X 3 ) on specific activity, temperature stability, storage stability and surfactant agent stability of pectinase from pitaya peel was investigated. The study demonstrated that the optimum conditions for the extraction of pectinase from pitaya sources could improve the enzymatic characteristics of the enzyme and protect its activity and stability during the extraction procedure. The optimum extraction conditions cause the pectinase to achieve high specific activity (15.31 U/mg), temperature stability (78%), storage stability (88%) and surfactant agent stability (83%). The most desirable conditions to achieve the highest activity and stability of pectinase enzyme from pitaya peel were the use of 5:1 buffer to sample ratio at 5 °C and pH 8.0.

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Cloning, purification and biochemical properties of a thermostable pectinase from Bacillus halodurans M29

Cited by 37 publications

References 23 publications

Assessment of pectinase production by Bacillus mojavensis I4 using an economical substrate and its potential application in oil sesame extraction

Assessment of pectinase production by Bacillus mojavensis I4 using an economical substrate and its potential application in oil sesame extraction

Characterization, Kinetic, and Thermodynamic Studies of Marine Pectinase FromBacillus subtilis

Optimization of Extraction of Novel Pectinase Enzyme Discovered in Red Pitaya (Hylocereus polyrhizus) Peel

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